Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Cockayne syndrome protein A in complex with DNA damage-binding protein 1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):45-8. doi: 10.1107/S1744309111045842. Epub 2011 Dec 24.

Abstract

Cockayne syndrome protein A is one of the main components in mammalian transcription coupled repair. Here, the overproduction, purification and crystallization of human Cockayne syndrome protein A in complex with its interacting partner DNA damage binding protein 1 are reported. The complex was coproduced in insect cells, copurified and crystallized using sitting drops with PEG 3350 and sodium citrate as crystallizing agents. The crystals had unit-cell parameters a = b = 142.03, c = 250.19 Å and diffracted to 2.9 Å resolution on beamline ID14-1 at the European Synchrotron Radiation Facility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • DNA Repair Enzymes / chemistry*
  • DNA Repair Enzymes / isolation & purification
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / isolation & purification
  • Humans
  • Protein Binding
  • Transcription Factors / chemistry*
  • Transcription Factors / isolation & purification

Substances

  • DDB1 protein, human
  • DNA-Binding Proteins
  • ERCC8 protein, human
  • Transcription Factors
  • DNA Repair Enzymes